issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

July 2005 issue

Highlighted illustration

Cover illustration: The structure of air-oxidized P. abyssi rubredoxin mutant W4L/R5S solved by direct methods and refined by partially restrained full-matrix least-squares refinement to 0.69 Å resolution (p. 990).

obituaries


research papers


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A robust method for determining bulk-solvent and anisotropic scaling parameters for macromolecular refinement is described. A maximum-likelihood target function for determination of flat bulk-solvent model parameters and overall anisotropic scale factor is also proposed.

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This work reports the structure of human PNP in complex with guanosine (at 2.80 Å resolution), 3′-deoxyguanosine (at 2.86 Å resolution) and 8-azaguanine (at 2.85 Å resolution). These structures were compared with the PNP–guanine, PNP–inosine and PNP–immucillin-H complexes solved previously.



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Protein crystals were successfully cryocooled by a He-gas high-pressure cooling method without any penetrative cryoprotectants. Excellent diffraction was observed. This method eliminates the need for penetrative cryoprotectants, thereby facilitating crystallographic data collection.

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Small changes in temperatures during flash-cooling have significant effects on the diffraction quality of nucleosome crystals and in some cases cause substantial changes in unit-cell parameters that are a result of the reorganization of molecules in the lattice. Thus, in cases where flash-cooling around liquid-nitrogen temperatures leads to a deterioration in diffraction, flash-cooling at intermediate temperatures using alternative cryogens may be a useful approach.

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Analysis shows that merging isomorphous replacement data with a limited number of highly accurate phases from the reference-beam diffraction experiment would significantly improve conventional experimental phasing.

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The crystal structure of PEP carboxykinase from a succinate-producing bacterium has been solved in the native form and in complex with pyruvate, manganese and phosphate. The structure of the complex reveals 2-mercaptoethanol covalently bound to a cysteine residue located within a previously unreported conserved motif in the active-site cleft. This motif also contains an important interdomain connection.

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Apo and cofactor-bound structures of T. thermophilus uroporphyrinogen-III C-methyltransferase solved to 2.0 Å resolution. These structures represent the `closed' form of the protein.


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An incorrect HslV-HslU quaternary structure can result from two biologically functional complexes sitting at the interface of two coherently associated lattices.

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The crystal structure of glycosylated interleukin-22 has been determined at 2.6 Å resolution. The structure provides new insights into IL-22 receptor recognition.

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A method and a software suite based on it are described for searching both program and parameter space to find the best solution for a given X-ray diffraction data set of protein crystals.


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Structures of several proteins were solved from crystals that exhibited phenomena such as the simultaneous presence of two lattice types, pseudosymmetry accompanied by twinning and unusual types of non-isomorphism.

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The statistical Shake-and-Bake procedure is optimized for Se-atom substructure determination.

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The reflection profiles from glycerol kinase crystals were analyzed using highly monochromatic parallel synchrotron radiation and fine φ-slicing to elucidate the effects of flash-cooling on diffraction quality.

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The structure of air-oxidized P. abyssi rubredoxin mutant W4L/R5S was solved by direct methods and refined by partially restrained full-matrix least-squares refinement to 0.69 Å resolution.

short communications



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The 1.5 Å resolution crystallographic structure of a 6 bp DNA in complex with ellipticine confirms the intercalative binding previously described in a self-complementary ribodinucleoside monophosphate and enables an accurate measurement of the distortion effects of the drug on real DNA.
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